Abstract
A heterologous radioreceptor assay was developed to follow the purification of an EGF-like polypeptide from bovine kidney. Purification of the growth factor was facilitated by the use of a novel affinity column using fixed A431 cells attached to sephadex beads. The mol. wt. of the purified EGF-LP was estimated to be 5480 from the amino acid composition. The purified EGF-like polypeptide stimulated the proliferation of bovine mammary epithelial cells and appeared to be equipotent to mouse EGF. Available evidence suggests that the purified molecule is distinct from bovine TGF-alpha.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1179-1187 |
| Number of pages | 9 |
| Journal | Biochemistry International |
| Volume | 20 |
| Issue number | 6 |
| State | Published - 1990 |
| Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry